Efficient large-scale purification of non-histone chromosomal proteins HMG1 and HMG2 by using Polybuffer-exchanger PBE94.
A method for the efficient and practical large-scale purification of high-mobility group (HMG) non-histone chromosomal proteins, HMG1 and HMG2, from porcine thymus applying Polybuffer-exchanger PBE94 gel as anion-exchanger has been developed. This method affords higher resolution, purity and yield, than the conventional procedure of CM-Sephadex C-25 ion-exchange column chromatography. Furthermore, use of Polybuffer-exchanger PBE94 column chromatography led to direct preparation of HMG1 and HMG2 from loosely bound non-histone chromosomal protein fraction of chromatin without prefractional precipitation with trichloroacetic acid or prior extraction with perchloric acid. Thus, the application of PBE94 gel as an anion-exchanger to the subfractionation of other kinds of homologous protein is possible.
Adachi
Y
Y
Department of Molecular Virology, Kyoto University, Japan.
Mizuno
S
S
Yoshida
M
M
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002021:Buffers; D002852:Chromatography, Ion Exchange / Q000379:methods*; D006609:High Mobility Group Proteins / Q000302:isolation & purification*; D007475:Ion Exchange Resins; D013552:Swine; D013950:Thymus Gland / Q000737:chemistry*
D000596:Amino Acids; D002021:Buffers; D006609:High Mobility Group Proteins; D007475:Ion Exchange Resins